hypothetical protein COS12_00470 [Candidatus Roizmanbacteria bacterium CG01_land_8_20_14_3_00_33_9]
Protein Classification
hexokinase family protein( domain architecture ID 19234154)
hexokinase family protein similar to Saccharomyces cerevisiae N-acetylglucosamine (GlcNAc) kinase that transfers a phosphate onto GlcNAc to generate GlcNAc-6-phosphate, which can be a precursor for glycan synthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| ASKHA_NBD_HK | cd24000 | nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
14-365 | 2.98e-57 | ||||||
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. : Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 190.18 E-value: 2.98e-57
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| Name | Accession | Description | Interval | E-value | |||||||
| ASKHA_NBD_HK | cd24000 | nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
14-365 | 2.98e-57 | |||||||
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 190.18 E-value: 2.98e-57
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| COG5026 | COG5026 | Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
11-362 | 1.21e-38 | |||||||
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 142.79 E-value: 1.21e-38
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| Hexokinase_2 | pfam03727 | Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
210-362 | 1.67e-15 | |||||||
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains. Pssm-ID: 461028 Cd Length: 236 Bit Score: 74.84 E-value: 1.67e-15
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| PLN02362 | PLN02362 | hexokinase |
62-250 | 2.08e-09 | |||||||
hexokinase Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 58.74 E-value: 2.08e-09
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| Name | Accession | Description | Interval | E-value | |||||||
| ASKHA_NBD_HK | cd24000 | nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
14-365 | 2.98e-57 | |||||||
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 190.18 E-value: 2.98e-57
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| COG5026 | COG5026 | Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
11-362 | 1.21e-38 | |||||||
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 142.79 E-value: 1.21e-38
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| Hexokinase_2 | pfam03727 | Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
210-362 | 1.67e-15 | |||||||
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains. Pssm-ID: 461028 Cd Length: 236 Bit Score: 74.84 E-value: 1.67e-15
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| ASKHA_NBD_HK_fungi | cd24018 | nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
15-362 | 7.84e-10 | |||||||
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. Pssm-ID: 466868 [Multi-domain] Cd Length: 431 Bit Score: 59.96 E-value: 7.84e-10
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| PLN02362 | PLN02362 | hexokinase |
62-250 | 2.08e-09 | |||||||
hexokinase Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 58.74 E-value: 2.08e-09
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| ASKHA_NBD_HK_meta | cd24019 | nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
100-362 | 6.66e-08 | |||||||
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. Pssm-ID: 466869 [Multi-domain] Cd Length: 427 Bit Score: 54.09 E-value: 6.66e-08
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| PLN02405 | PLN02405 | hexokinase |
16-250 | 1.02e-07 | |||||||
hexokinase Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 53.68 E-value: 1.02e-07
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| ASKHA_NBD_GLK1-2_fungi | cd24088 | nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
210-250 | 4.00e-07 | |||||||
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 (GLK-2) from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (also known as glucokinase-1, EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to glucokinase-1 and glucokinase-2. Pssm-ID: 466938 [Multi-domain] Cd Length: 445 Bit Score: 51.63 E-value: 4.00e-07
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| PTZ00107 | PTZ00107 | hexokinase; Provisional |
210-362 | 4.83e-07 | |||||||
hexokinase; Provisional Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 51.22 E-value: 4.83e-07
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| ASKHA_NBD_HK1-2_fungi | cd24087 | nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
16-250 | 3.17e-06 | |||||||
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively. Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 48.91 E-value: 3.17e-06
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| ASKHA_NBD_HK_plant | cd24020 | nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
210-250 | 8.59e-06 | |||||||
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth. Pssm-ID: 466870 [Multi-domain] Cd Length: 439 Bit Score: 47.27 E-value: 8.59e-06
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| PLN02914 | PLN02914 | hexokinase |
115-250 | 1.62e-05 | |||||||
hexokinase Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 46.80 E-value: 1.62e-05
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| ASKHA_NBD_HK1_meta_rpt1 | cd24124 | nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
12-362 | 1.47e-04 | |||||||
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase. Pssm-ID: 466974 [Multi-domain] Cd Length: 473 Bit Score: 43.45 E-value: 1.47e-04
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| ASKHA_NBD_HK1-2_meta_rpt1 | cd24089 | nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
98-362 | 5.69e-04 | |||||||
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of types I and II hexokinases. Pssm-ID: 466939 [Multi-domain] Cd Length: 429 Bit Score: 41.68 E-value: 5.69e-04
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| PLN02596 | PLN02596 | hexokinase-like |
210-250 | 6.53e-04 | |||||||
hexokinase-like Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 41.40 E-value: 6.53e-04
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| ASKHA_NBD_HKDC1_meta_rpt1 | cd24126 | nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
13-362 | 9.73e-04 | |||||||
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the first two domains of HKDC1. Pssm-ID: 466976 [Multi-domain] Cd Length: 429 Bit Score: 40.99 E-value: 9.73e-04
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| ASKHA_NBD_HK2_meta_rpt1 | cd24125 | nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
12-362 | 4.27e-03 | |||||||
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type II hexokinase. Pssm-ID: 466975 [Multi-domain] Cd Length: 429 Bit Score: 38.72 E-value: 4.27e-03
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